ID A0A2Y9N7W1_DELLE Unreviewed; 1911 AA.
AC A0A2Y9N7W1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Bromodomain adjacent to zinc finger domain protein 2A isoform X4 {ECO:0000313|RefSeq:XP_022427517.1, ECO:0000313|RefSeq:XP_022427518.1};
GN Name=BAZ2A {ECO:0000313|RefSeq:XP_022427517.1,
GN ECO:0000313|RefSeq:XP_022427518.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022427517.1};
RN [1] {ECO:0000313|RefSeq:XP_022427517.1, ECO:0000313|RefSeq:XP_022427518.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022427517.1,
RC ECO:0000313|RefSeq:XP_022427518.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000256|ARBA:ARBA00007444}.
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DR RefSeq; XP_022427517.1; XM_022571809.1.
DR RefSeq; XP_022427518.1; XM_022571810.2.
DR Ensembl; ENSDLET00000008258; ENSDLEP00000007465; ENSDLEG00000005511.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd05503; Bromo_BAZ2A_B_like; 1.
DR CDD; cd01397; HAT_MBD; 1.
DR CDD; cd15629; PHD_BAZ2A; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR037374; BAZ2A/B_Bromo.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR028940; PHD_BAZ2A.
DR InterPro; IPR028942; WHIM1_dom.
DR InterPro; IPR028941; WHIM2_dom.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45915:SF5; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 2A; 1.
DR PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF02791; DDT; 1.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF15612; WHIM1; 1.
DR Pfam; PF15613; WSD; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00384; AT_hook; 4.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00571; DDT; 1.
DR SMART; SM00391; MBD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF54171; DNA-binding domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 549..620
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 851..916
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1683..1733
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1816..1886
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1160..1269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1773..1796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 739..769
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1053
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1160..1189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1208..1250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1309..1323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1340..1363
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1364..1384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1911 AA; 211594 MW; 6DAC8ABEB89D1025 CRC64;
MEANDHFNFT GLPPAPAASG LKPSPSSGEG LYTNGSPMNF PQQGKSLNGD VNVNGLSTVS
HTTTSGILNS APHSSSTSHL HHPNVAYDCL WNYSQYPPAN PGSNLKDPPL LSQFSGGQYP
LNGILGGSRQ PSSPSHNTNL RAGSQEFWAN GTQSPMGLNF DSQELYDSFP DQNFEVMPNG
PPSFFTSPQT SPMLGSSIQT FAPSQEVGSG IHPDEAAEKE LTSVVAENGT GLVGSLELEE
EQPELKMCGY NGSVPSVESL HQEVSVLVPD PTVSCLDDPS HLSDQLEDTP ILSEVSLEPF
NTLAPEPVTG GLYGIDDTEL MGAEDKLPLE DSPVISALDC PSLNNATAFS LLADDSQTSA
SIFASPTSPP VLGESVLQDT SFDLNNGSDA EQEEMETQAS EFPPSLTQPA PDQSSTLQLR
TAASPAVSPT ALPAVSLAVS PAASPEISPE VSPAASPEIS PAISPAAFPT VSPTSSAALP
PVSSEVSLTA SPVTSPKASP APSPAAVFPA ASPADKNVSS FLETTADLEE ITGEGVTPSG
SGDVLRRRIA TPEEVRLPLQ HGWRREVRIK KGSHRWQGET WYYGPCGKRM KQFPEVIKYL
SRNVVHNVRR EHFSFSPRMP VGDFFEERDT PEGLQWVQLS AEEIPSRIQA ITGKRGRPRN
TEKAKTKDVP KVKRGRGRPP KVKITELLNK TDNRLLKKLE AQETLNEEDK SKMSKIKKKM
KQKVQRGECQ TTNQGQAKSK RKQETKSLKQ KEAKKKLKAE KEKVKTKQEK LKEKVKREKK
EKVKMKEKEE VAKAKPACKA DKALATQRRF EERQRQQMIL EEMKKPTEDM CLTDHQPLPD
FSRIPSLILP SGAFSDCLTI VEFLHSFGKV LGFDPAKDVP SLGVLQEGLL CQGDSLGEVQ
DLLVRLLKAA LYDPGLPSYC QSLKILGEKV SEIPLTRDNV SEILRCFLMA YGVEPALCDS
LRTQPFQAQP PQQKAAVLAF LVHELNGSTL IINEIDKTLE SMSSYRKNKW IVEGRLRRLK
TALAKRTGRP EVELQGPEEG LGRRRSSRIM EETSGMEEEE EEETTAAVHG RRGRRDGEVD
VIASSIPELE RQIEKLSKRQ LFFRKKLLHS SQMLRAVSLG QDRYRRNYWV LPYLTGIFVE
GTEGSLVPED VIKQETDSLK VATHSTPSPA SFSLKRELAG SSTSASSPAR ARGRPRKTKP
GSVQPRHLKS PVKSQGSEEL QVQLQPETQP HPQLQAHAQP QPQLQSHPHS HNGFLEPEGS
PLSLGQSQHD LSQSAFLSWL SQTQSHGSLL SSSVLTPDSS PGKLDPMPSR PPEEPEPDER
EASPDSQAPW FNFSAQMPCS AAPTPPPAVS EDHPTPSPQL PASSKPVNRP SAANPYSPVQ
LSSTPLLGMA PKRRAGDPRE TPQSPTGMGQ PKRRGRPPSK FFKQMEQRYL TQLTAQPVPP
EMRSGWWWIR DPETLDAMLK ALHPRGIREK ALHKHLNKHR DFLQEVCLRP STDPIFEPSQ
LLAFQEGITS WSPKEKTYET DLAVLQWVEE LEQRVILSDL QIRGWTRPSP DSTREDLAYC
EHLPDSQEDI TWRGRGKEGL APQRKTTNPL DLAVTRLAAL EQNVERRYLR EPLWPAHEVV
LEKALLGTPS SAPQCATAEI SYEITPRIRA WRQTLERCWS AAQVCLCLGQ LERSIAWEKS
VNKVTCLVCR KGDNDEFLLL CDGCDRGCHI YCLRPKMEAV PEGDWFCAVC LAQQVEGELT
QRPGFPKRGQ KRKSSYVLNF PEGDSCRRRL LSRGRESPAV PRCSEGGQSP SKRRRLSMRN
HHSDLTFCEI ILMEMESHDA AWPFLEPVNP RLVSGYRRII KNPMDFSTMR ERLLRGGYTS
SEEFAADALL VFDNCQTFNE DDSEVGKAGH IMRRFFESRW EEFYQGKQAN L
//
